data_4444 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C and 15N chemical shift assignments and secondary structure of Halobacterium salinarum ferredoxin ; _BMRB_accession_number 4444 _BMRB_flat_file_name bmr4444.str _Entry_type original _Submission_date 1999-10-20 _Accession_date 1999-10-20 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Schweimer Kristian . . 2 Marg Bianca-Lucia . . 3 Oesterhelt Dieter . . 4 Roesch Paul . . 5 Sticht Heinrich . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 519 "13C chemical shifts" 349 "15N chemical shifts" 111 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-07-28 update BMRB 'Updating non-standard residue' 2000-04-03 original author . stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: Sequence-specific 1H, 13C and 15N resonance assignments and secondary structure of [2Fe-2S] ferredoxin from Halobacterium salinarum ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Schweimer Kristian . . 2 Marg Bianca-Lucia . . 3 Oesterhelt Dieter . . 4 Roesch Paul . . 5 Sticht Heinrich . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 16 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 347 _Page_last 348 _Year 2000 _Details . save_ ################################## # Molecular system description # ################################## save_Fdx _Saveframe_category molecular_system _Mol_system_name Ferredoxin _Abbreviation_common Fdx _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'HsFdx monomer' $HsFdx 2Fe-2S $FES stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic yes _System_thiol_state 'all bound' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_HsFdx _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'halobacterium salinarum ferredoxin' _Abbreviation_common HsFdx _Molecular_mass . _Mol_thiol_state 'all bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 128 _Mol_residue_sequence ; PTVEYLNYETLDDQGWDMDD DDLFEKAADAGLDGEDYGTM EVAEGEYILEAAEAQGYDWP FSCRAGACANCASIVKEGEI DMDMQQILSDEEVEEKDVRL TCIGSPAADEVKIVYNAXHL DYLQNRVI ; loop_ _Residue_seq_code _Residue_label 1 PRO 2 THR 3 VAL 4 GLU 5 TYR 6 LEU 7 ASN 8 TYR 9 GLU 10 THR 11 LEU 12 ASP 13 ASP 14 GLN 15 GLY 16 TRP 17 ASP 18 MET 19 ASP 20 ASP 21 ASP 22 ASP 23 LEU 24 PHE 25 GLU 26 LYS 27 ALA 28 ALA 29 ASP 30 ALA 31 GLY 32 LEU 33 ASP 34 GLY 35 GLU 36 ASP 37 TYR 38 GLY 39 THR 40 MET 41 GLU 42 VAL 43 ALA 44 GLU 45 GLY 46 GLU 47 TYR 48 ILE 49 LEU 50 GLU 51 ALA 52 ALA 53 GLU 54 ALA 55 GLN 56 GLY 57 TYR 58 ASP 59 TRP 60 PRO 61 PHE 62 SER 63 CYS 64 ARG 65 ALA 66 GLY 67 ALA 68 CYS 69 ALA 70 ASN 71 CYS 72 ALA 73 SER 74 ILE 75 VAL 76 LYS 77 GLU 78 GLY 79 GLU 80 ILE 81 ASP 82 MET 83 ASP 84 MET 85 GLN 86 GLN 87 ILE 88 LEU 89 SER 90 ASP 91 GLU 92 GLU 93 VAL 94 GLU 95 GLU 96 LYS 97 ASP 98 VAL 99 ARG 100 LEU 101 THR 102 CYS 103 ILE 104 GLY 105 SER 106 PRO 107 ALA 108 ALA 109 ASP 110 GLU 111 VAL 112 LYS 113 ILE 114 VAL 115 TYR 116 ASN 117 ALA 118 ALY 119 HIS 120 LEU 121 ASP 122 TYR 123 LEU 124 GLN 125 ASN 126 ARG 127 VAL 128 ILE stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-13 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 1E0Z "[2fe-2s]-Ferredoxin From Halobacterium Salinarum" 100.00 128 100.00 100.00 2.80e-85 PDB 1E10 "[2fe-2s]-Ferredoxin From Halobacterium Salinarum" 99.22 128 99.21 99.21 3.27e-84 EMBL CAA48224 "ferredoxin [Halobacterium salinarum]" 100.00 129 99.22 99.22 1.55e-85 EMBL CAP14708 "ferredoxin (2Fe-2S) [Halobacterium salinarum R1]" 100.00 129 99.22 99.22 1.55e-85 GB AAG20406 "ferredoxin [Halobacterium sp. NRC-1]" 100.00 129 99.22 99.22 1.55e-85 PRF 0407261A ferredoxin 100.00 128 99.22 99.22 2.33e-85 PRF 1916400A "2Fe2S ferredoxin" 100.00 129 99.22 99.22 1.55e-85 REF WP_010903707 "ferredoxin [Halobacterium salinarum]" 100.00 129 99.22 99.22 1.55e-85 SP P00216 "RecName: Full=Ferredoxin" 100.00 129 99.22 99.22 1.55e-85 stop_ save_ ###################### # Polymer residues # ###################### save_chem_comp_ALY _Saveframe_category polymer_residue _Mol_type 'L-peptide linking' _Name_common N(6)-ACETYLLYSINE _BMRB_code . _PDB_code ALY _Standard_residue_derivative . _Molecular_mass 188.224 _Mol_paramagnetic . _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Mon Jul 18 10:13:56 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons OH OH O . 0 . ? CH CH C . 0 . ? CH3 CH3 C . 0 . ? NZ NZ N . 0 . ? CE CE C . 0 . ? CD CD C . 0 . ? CG CG C . 0 . ? CB CB C . 0 . ? CA CA C . 0 . ? N N N . 0 . ? C C C . 0 . ? O O O . 0 . ? OXT OXT O . 0 . ? HH31 HH31 H . 0 . ? HH32 HH32 H . 0 . ? HH33 HH33 H . 0 . ? HZ HZ H . 0 . ? HE3 HE3 H . 0 . ? HE2 HE2 H . 0 . ? HD3 HD3 H . 0 . ? HD2 HD2 H . 0 . ? HG3 HG3 H . 0 . ? HG2 HG2 H . 0 . ? HB3 HB3 H . 0 . ? HB2 HB2 H . 0 . ? HCA HCA H . 0 . ? H H H . 0 . ? H2 H2 H . 0 . ? HXT HXT H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name DOUB OH CH ? ? SING CH CH3 ? ? SING CH NZ ? ? SING CH3 HH31 ? ? SING CH3 HH32 ? ? SING CH3 HH33 ? ? SING NZ CE ? ? SING NZ HZ ? ? SING CE CD ? ? SING CE HE3 ? ? SING CE HE2 ? ? SING CD CG ? ? SING CD HD3 ? ? SING CD HD2 ? ? SING CG CB ? ? SING CG HG3 ? ? SING CG HG2 ? ? SING CB CA ? ? SING CB HB3 ? ? SING CB HB2 ? ? SING CA N ? ? SING CA C ? ? SING CA HCA ? ? SING N H ? ? SING N H2 ? ? DOUB C O ? ? SING C OXT ? ? SING OXT HXT ? ? stop_ save_ ############# # Ligands # ############# save_FES _Saveframe_category ligand _Mol_type non-polymer _Name_common "FES (FE2/S2 (INORGANIC) CLUSTER)" _BMRB_code . _PDB_code FES _Molecular_mass 175.820 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Mon Jul 18 10:04:10 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons FE1 FE1 FE . 0 . ? FE2 FE2 FE . 0 . ? S1 S1 S . 0 . ? S2 S2 S . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING FE1 S1 ? ? SING FE1 S2 ? ? SING FE2 S1 ? ? SING FE2 S2 ? ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $HsFdx 'Halobacterium salinarum' 2242 Archaea Euryarchaeota Halobacterium salinarum stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $HsFdx 'purified from the natural source' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $HsFdx 0.9 mM '[U-99% 13C; U-99% 15N]' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $HsFdx 1.0 mM '[U-99% 15N]' stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $HsFdx 0.8 mM . stop_ save_ ############################ # Computer software used # ############################ save_NMRView _Saveframe_category software _Name NMRView _Version 4.0.1 loop_ _Task ; spectrum visualization for resonance assignments ; stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label . save_ save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details ; HNCO HNCA HNCACB CBCA(CO)NH HNHA HBHA(CO)NH HCCH-COSY HCCH-TOCSY 1H-15N-HSQC 1H-13C CT-HSQC ; save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.5 0.2 n/a temperature 288 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 $entry_citation $entry_citation DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 $entry_citation $entry_citation stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'HsFdx monomer' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 1 PRO HA H 4.60 0.02 . 2 . 1 PRO C C 171.38 0.15 . 3 . 1 PRO CA C 63.31 0.15 . 4 . 1 PRO CB C 32.10 0.15 . 5 . 2 THR H H 8.87 0.02 . 6 . 2 THR HA H 4.96 0.02 . 7 . 2 THR HB H 4.08 0.02 . 8 . 2 THR HG2 H 1.21 0.02 . 9 . 2 THR C C 173.36 0.15 . 10 . 2 THR CA C 62.03 0.15 . 11 . 2 THR CB C 70.71 0.15 . 12 . 2 THR CG2 C 21.90 0.15 . 13 . 2 THR N N 119.16 0.1 . 14 . 3 VAL H H 9.38 0.02 . 15 . 3 VAL HA H 4.91 0.02 . 16 . 3 VAL HB H 2.11 0.02 . 17 . 3 VAL HG1 H 1.00 0.02 . 18 . 3 VAL HG2 H 0.87 0.02 . 19 . 3 VAL C C 173.63 0.15 . 20 . 3 VAL CA C 61.04 0.15 . 21 . 3 VAL CB C 33.93 0.15 . 22 . 3 VAL N N 126.26 0.1 . 23 . 4 GLU H H 9.35 0.02 . 24 . 4 GLU HA H 5.28 0.02 . 25 . 4 GLU HB2 H 1.89 0.02 . 26 . 4 GLU HB3 H 1.89 0.02 . 27 . 4 GLU HG2 H 2.26 0.02 . 28 . 4 GLU HG3 H 2.26 0.02 . 29 . 4 GLU C C 174.66 0.15 . 30 . 4 GLU CA C 54.28 0.15 . 31 . 4 GLU CB C 31.99 0.15 . 32 . 4 GLU N N 133.73 0.1 . 33 . 5 TYR H H 8.64 0.02 . 34 . 5 TYR HA H 6.43 0.02 . 35 . 5 TYR HB2 H 2.70 0.02 . 36 . 5 TYR HB3 H 3.10 0.02 . 37 . 5 TYR HD1 H 6.80 0.02 . 38 . 5 TYR HD2 H 6.80 0.02 . 39 . 5 TYR HE1 H 6.73 0.02 . 40 . 5 TYR HE2 H 6.73 0.02 . 41 . 5 TYR C C 172.80 0.15 . 42 . 5 TYR CA C 54.52 0.15 . 43 . 5 TYR CB C 44.12 0.15 . 44 . 5 TYR N N 123.93 0.1 . 45 . 6 LEU H H 8.33 0.02 . 46 . 6 LEU HA H 5.76 0.02 . 47 . 6 LEU HB2 H 1.46 0.02 . 48 . 6 LEU HB3 H 1.46 0.02 . 49 . 6 LEU HD1 H 0.43 0.02 . 50 . 6 LEU HD2 H 1.17 0.02 . 51 . 6 LEU C C 176.03 0.15 . 52 . 6 LEU CA C 53.26 0.15 . 53 . 6 LEU CB C 48.41 0.15 . 54 . 6 LEU CD1 C 27.11 0.15 . 55 . 6 LEU CD2 C 23.80 0.15 . 56 . 6 LEU N N 118.58 0.1 . 57 . 7 ASN H H 9.36 0.02 . 58 . 7 ASN HA H 3.21 0.02 . 59 . 7 ASN HB2 H 3.42 0.02 . 60 . 7 ASN HB3 H 2.97 0.02 . 61 . 7 ASN HD21 H 7.43 0.02 . 62 . 7 ASN HD22 H 7.92 0.02 . 63 . 7 ASN C C 176.00 0.15 . 64 . 7 ASN CA C 53.52 0.15 . 65 . 7 ASN CB C 38.33 0.15 . 66 . 7 ASN N N 127.41 0.1 . 67 . 7 ASN ND2 N 113.83 0.1 . 68 . 8 TYR H H 9.03 0.02 . 69 . 8 TYR HA H 3.72 0.02 . 70 . 8 TYR HB2 H 2.68 0.02 . 71 . 8 TYR HB3 H 2.96 0.02 . 72 . 8 TYR HD1 H 6.79 0.02 . 73 . 8 TYR HD2 H 6.79 0.02 . 74 . 8 TYR HE1 H 6.72 0.02 . 75 . 8 TYR HE2 H 6.72 0.02 . 76 . 8 TYR C C 177.24 0.15 . 77 . 8 TYR CA C 62.55 0.15 . 78 . 8 TYR CB C 40.69 0.15 . 79 . 8 TYR N N 131.21 0.1 . 80 . 9 GLU H H 8.13 0.02 . 81 . 9 GLU HA H 3.67 0.02 . 82 . 9 GLU HB2 H 2.33 0.02 . 83 . 9 GLU HB3 H 2.33 0.02 . 84 . 9 GLU C C 177.53 0.15 . 85 . 9 GLU CA C 59.22 0.15 . 86 . 9 GLU CB C 29.94 0.15 . 87 . 9 GLU N N 114.75 0.1 . 88 . 10 THR H H 7.61 0.02 . 89 . 10 THR HA H 3.88 0.02 . 90 . 10 THR HB H 4.10 0.02 . 91 . 10 THR HG2 H 1.25 0.02 . 92 . 10 THR C C 175.93 0.15 . 93 . 10 THR CA C 64.98 0.15 . 94 . 10 THR CB C 69.41 0.15 . 95 . 10 THR N N 113.61 0.1 . 96 . 11 LEU H H 7.25 0.02 . 97 . 11 LEU HA H 3.69 0.02 . 98 . 11 LEU HB2 H 1.55 0.02 . 99 . 11 LEU HB3 H 1.55 0.02 . 100 . 11 LEU HD1 H 0.78 0.02 . 101 . 11 LEU HD2 H 0.83 0.02 . 102 . 11 LEU C C 178.95 0.15 . 103 . 11 LEU CA C 60.21 0.15 . 104 . 11 LEU CB C 39.66 0.15 . 105 . 11 LEU CD1 C 26.00 0.15 . 106 . 11 LEU N N 121.41 0.1 . 107 . 12 ASP H H 7.93 0.02 . 108 . 12 ASP HA H 4.30 0.02 . 109 . 12 ASP HB2 H 2.47 0.02 . 110 . 12 ASP HB3 H 2.47 0.02 . 111 . 12 ASP C C 178.91 0.15 . 112 . 12 ASP CA C 57.31 0.15 . 113 . 12 ASP CB C 41.16 0.15 . 114 . 12 ASP N N 118.22 0.1 . 115 . 13 ASP H H 7.28 0.02 . 116 . 13 ASP HA H 4.21 0.02 . 117 . 13 ASP HB2 H 2.51 0.02 . 118 . 13 ASP HB3 H 2.51 0.02 . 119 . 13 ASP C C 177.84 0.15 . 120 . 13 ASP CA C 57.23 0.15 . 121 . 13 ASP CB C 41.43 0.15 . 122 . 13 ASP N N 118.98 0.1 . 123 . 14 GLN H H 7.32 0.02 . 124 . 14 GLN HA H 3.61 0.02 . 125 . 14 GLN HB3 H 0.40 0.02 . 126 . 14 GLN HG2 H 1.85 0.02 . 127 . 14 GLN HG3 H 1.85 0.02 . 128 . 14 GLN HE21 H 6.77 0.02 . 129 . 14 GLN HE22 H 7.11 0.02 . 130 . 14 GLN C C 171.00 0.15 . 131 . 14 GLN CA C 54.78 0.15 . 132 . 14 GLN CB C 26.70 0.15 . 133 . 14 GLN N N 113.92 0.1 . 134 . 14 GLN NE2 N 112.75 0.1 . 135 . 15 GLY H H 7.51 0.02 . 136 . 15 GLY HA2 H 3.90 0.02 . 137 . 15 GLY HA3 H 3.90 0.02 . 138 . 15 GLY C C 175.25 0.15 . 139 . 15 GLY CA C 46.15 0.15 . 140 . 15 GLY N N 108.37 0.1 . 141 . 16 TRP H H 7.92 0.02 . 142 . 16 TRP HA H 5.11 0.02 . 143 . 16 TRP HB2 H 2.87 0.02 . 144 . 16 TRP HB3 H 3.05 0.02 . 145 . 16 TRP HD1 H 6.97 0.02 . 146 . 16 TRP HE1 H 10.29 0.02 . 147 . 16 TRP HE3 H 6.56 0.02 . 148 . 16 TRP HZ2 H 6.96 0.02 . 149 . 16 TRP HZ3 H 6.82 0.02 . 150 . 16 TRP HH2 H 6.38 0.02 . 151 . 16 TRP C C 173.98 0.15 . 152 . 16 TRP CA C 53.48 0.15 . 153 . 16 TRP CB C 31.90 0.15 . 154 . 16 TRP N N 121.72 0.1 . 155 . 17 ASP H H 8.52 0.02 . 156 . 17 ASP HA H 4.93 0.02 . 157 . 17 ASP HB2 H 2.56 0.02 . 158 . 17 ASP HB3 H 2.81 0.02 . 159 . 17 ASP C C 175.98 0.15 . 160 . 17 ASP CA C 53.03 0.15 . 161 . 17 ASP CB C 45.80 0.15 . 162 . 17 ASP N N 121.81 0.1 . 163 . 18 MET H H 8.79 0.02 . 164 . 18 MET HA H 4.11 0.02 . 165 . 18 MET HB2 H 2.15 0.02 . 166 . 18 MET HB3 H 2.15 0.02 . 167 . 18 MET C C 175.90 0.15 . 168 . 18 MET CA C 57.87 0.15 . 169 . 18 MET CB C 33.54 0.15 . 170 . 18 MET N N 124.37 0.1 . 171 . 19 ASP H H 8.65 0.02 . 172 . 19 ASP HA H 4.76 0.02 . 173 . 19 ASP HB2 H 2.60 0.02 . 174 . 19 ASP HB3 H 2.89 0.02 . 175 . 19 ASP C C 176.45 0.15 . 176 . 19 ASP CA C 54.07 0.15 . 177 . 19 ASP CB C 40.82 0.15 . 178 . 19 ASP N N 115.71 0.1 . 179 . 20 ASP H H 7.93 0.02 . 180 . 20 ASP HA H 4.47 0.02 . 181 . 20 ASP HB2 H 2.75 0.02 . 182 . 20 ASP HB3 H 2.75 0.02 . 183 . 20 ASP C C 178.63 0.15 . 184 . 20 ASP CA C 55.46 0.15 . 185 . 20 ASP CB C 40.64 0.15 . 186 . 20 ASP N N 122.91 0.1 . 187 . 21 ASP H H 9.21 0.02 . 188 . 21 ASP HA H 4.48 0.02 . 189 . 21 ASP HB2 H 2.74 0.02 . 190 . 21 ASP HB3 H 2.74 0.02 . 191 . 21 ASP C C 176.80 0.15 . 192 . 21 ASP CA C 56.69 0.15 . 193 . 21 ASP CB C 40.72 0.15 . 194 . 21 ASP N N 127.99 0.1 . 195 . 22 ASP H H 8.51 0.02 . 196 . 22 ASP HA H 4.91 0.02 . 197 . 22 ASP HB2 H 2.56 0.02 . 198 . 22 ASP HB3 H 2.89 0.02 . 199 . 22 ASP C C 176.46 0.15 . 200 . 22 ASP CA C 52.27 0.15 . 201 . 22 ASP CB C 39.90 0.15 . 202 . 22 ASP N N 117.68 0.1 . 203 . 23 LEU H H 7.09 0.02 . 204 . 23 LEU HA H 3.24 0.02 . 205 . 23 LEU HB2 H 1.43 0.02 . 206 . 23 LEU HB3 H 1.71 0.02 . 207 . 23 LEU HD1 H 0.63 0.02 . 208 . 23 LEU HD2 H 0.73 0.02 . 209 . 23 LEU C C 176.51 0.15 . 210 . 23 LEU CA C 59.22 0.15 . 211 . 23 LEU CB C 43.19 0.15 . 212 . 23 LEU CD1 C 23.12 0.15 . 213 . 23 LEU CD2 C 25.66 0.15 . 214 . 23 LEU N N 120.23 0.1 . 215 . 24 PHE H H 8.34 0.02 . 216 . 24 PHE HA H 3.72 0.02 . 217 . 24 PHE HB2 H 2.81 0.02 . 218 . 24 PHE HB3 H 3.31 0.02 . 219 . 24 PHE HD1 H 7.47 0.02 . 220 . 24 PHE HD2 H 7.47 0.02 . 221 . 24 PHE HE1 H 7.18 0.02 . 222 . 24 PHE HE2 H 7.18 0.02 . 223 . 24 PHE HZ H 7.03 0.02 . 224 . 24 PHE C C 178.25 0.15 . 225 . 24 PHE CA C 62.48 0.15 . 226 . 24 PHE CB C 37.51 0.15 . 227 . 24 PHE N N 113.48 0.1 . 228 . 25 GLU H H 7.69 0.02 . 229 . 25 GLU HA H 3.92 0.02 . 230 . 25 GLU HB2 H 1.99 0.02 . 231 . 25 GLU HB3 H 1.99 0.02 . 232 . 25 GLU C C 179.17 0.15 . 233 . 25 GLU CA C 59.81 0.15 . 234 . 25 GLU CB C 29.13 0.15 . 235 . 25 GLU N N 123.33 0.1 . 236 . 26 LYS H H 7.90 0.02 . 237 . 26 LYS HA H 3.80 0.02 . 238 . 26 LYS HB2 H 0.80 0.02 . 239 . 26 LYS HB3 H 0.99 0.02 . 240 . 26 LYS C C 180.21 0.15 . 241 . 26 LYS CA C 59.49 0.15 . 242 . 26 LYS CB C 30.82 0.15 . 243 . 26 LYS N N 119.45 0.1 . 244 . 27 ALA H H 7.46 0.02 . 245 . 27 ALA HA H 3.82 0.02 . 246 . 27 ALA HB H 0.78 0.02 . 247 . 27 ALA C C 178.91 0.15 . 248 . 27 ALA CA C 55.26 0.15 . 249 . 27 ALA CB C 18.93 0.15 . 250 . 27 ALA N N 122.69 0.1 . 251 . 28 ALA H H 7.27 0.02 . 252 . 28 ALA HA H 3.80 0.02 . 253 . 28 ALA HB H 1.52 0.02 . 254 . 28 ALA C C 179.10 0.15 . 255 . 28 ALA CA C 54.93 0.15 . 256 . 28 ALA CB C 18.33 0.15 . 257 . 28 ALA N N 118.94 0.1 . 258 . 29 ASP H H 7.16 0.02 . 259 . 29 ASP HA H 4.89 0.02 . 260 . 29 ASP HB2 H 2.49 0.02 . 261 . 29 ASP HB3 H 2.79 0.02 . 262 . 29 ASP C C 176.90 0.15 . 263 . 29 ASP CA C 54.43 0.15 . 264 . 29 ASP CB C 42.26 0.15 . 265 . 29 ASP N N 116.49 0.1 . 266 . 30 ALA H H 7.38 0.02 . 267 . 30 ALA HA H 4.44 0.02 . 268 . 30 ALA HB H 1.66 0.02 . 269 . 30 ALA C C 177.48 0.15 . 270 . 30 ALA CA C 53.41 0.15 . 271 . 30 ALA CB C 19.66 0.15 . 272 . 30 ALA N N 121.17 0.1 . 273 . 31 GLY H H 8.36 0.02 . 274 . 31 GLY HA2 H 3.95 0.02 . 275 . 31 GLY HA3 H 3.95 0.02 . 276 . 31 GLY C C 175.80 0.15 . 277 . 31 GLY CA C 47.17 0.15 . 278 . 31 GLY N N 111.22 0.1 . 279 . 32 LEU H H 8.95 0.02 . 280 . 32 LEU HA H 4.39 0.02 . 281 . 32 LEU HB2 H 1.78 0.02 . 282 . 32 LEU HB3 H 2.01 0.02 . 283 . 32 LEU C C 178.02 0.15 . 284 . 32 LEU CA C 54.19 0.15 . 285 . 32 LEU CB C 43.16 0.15 . 286 . 32 LEU N N 120.97 0.1 . 287 . 33 ASP H H 9.56 0.02 . 288 . 33 ASP HA H 4.78 0.02 . 289 . 33 ASP HB2 H 2.90 0.02 . 290 . 33 ASP HB3 H 2.96 0.02 . 291 . 33 ASP C C 178.17 0.15 . 292 . 33 ASP CA C 54.78 0.15 . 293 . 33 ASP CB C 42.70 0.15 . 294 . 33 ASP N N 124.21 0.1 . 295 . 34 GLY H H 9.00 0.02 . 296 . 34 GLY HA2 H 4.51 0.02 . 297 . 34 GLY HA3 H 4.10 0.02 . 298 . 34 GLY C C 175.14 0.15 . 299 . 34 GLY CA C 46.91 0.15 . 300 . 34 GLY N N 111.30 0.1 . 301 . 35 GLU H H 9.11 0.02 . 302 . 35 GLU HA H 3.60 0.02 . 303 . 35 GLU HB2 H 2.05 0.02 . 304 . 35 GLU HB3 H 2.05 0.02 . 305 . 35 GLU HG2 H 2.44 0.02 . 306 . 35 GLU HG3 H 2.44 0.02 . 307 . 35 GLU C C 178.52 0.15 . 308 . 35 GLU CA C 59.10 0.15 . 309 . 35 GLU CB C 29.83 0.15 . 310 . 35 GLU CG C 37.60 0.15 . 311 . 35 GLU N N 119.92 0.1 . 312 . 36 ASP H H 8.07 0.02 . 313 . 36 ASP HA H 5.15 0.02 . 314 . 36 ASP HB2 H 2.98 0.02 . 315 . 36 ASP HB3 H 2.98 0.02 . 316 . 36 ASP C C 175.39 0.15 . 317 . 36 ASP CA C 56.74 0.15 . 318 . 36 ASP CB C 43.41 0.15 . 319 . 36 ASP N N 119.78 0.1 . 320 . 37 TYR H H 8.03 0.02 . 321 . 37 TYR HA H 5.39 0.02 . 322 . 37 TYR HB2 H 2.38 0.02 . 323 . 37 TYR HB3 H 3.36 0.02 . 324 . 37 TYR HD1 H 7.21 0.02 . 325 . 37 TYR HD2 H 7.21 0.02 . 326 . 37 TYR HE1 H 6.96 0.02 . 327 . 37 TYR HE2 H 6.96 0.02 . 328 . 37 TYR C C 172.79 0.15 . 329 . 37 TYR CA C 57.38 0.15 . 330 . 37 TYR CB C 43.15 0.15 . 331 . 37 TYR N N 120.68 0.1 . 332 . 38 GLY H H 6.23 0.02 . 333 . 38 GLY HA2 H 3.94 0.02 . 334 . 38 GLY HA3 H 3.07 0.02 . 335 . 38 GLY C C 182.18 0.15 . 336 . 38 GLY CA C 45.05 0.15 . 337 . 38 GLY N N 114.94 0.1 . 338 . 39 THR H H 8.00 0.02 . 339 . 39 THR HA H 5.52 0.02 . 340 . 39 THR HB H 3.89 0.02 . 341 . 39 THR HG2 H 1.08 0.02 . 342 . 39 THR C C 174.08 0.15 . 343 . 39 THR CA C 59.87 0.15 . 344 . 39 THR CB C 72.04 0.15 . 345 . 39 THR CG2 C 21.90 0.15 . 346 . 39 THR N N 109.66 0.1 . 347 . 40 MET H H 9.21 0.02 . 348 . 40 MET HA H 4.97 0.02 . 349 . 40 MET HB2 H 1.96 0.02 . 350 . 40 MET HB3 H 2.16 0.02 . 351 . 40 MET HG2 H 2.24 0.02 . 352 . 40 MET HG3 H 2.37 0.02 . 353 . 40 MET HE H 1.53 0.02 . 354 . 40 MET C C 173.86 0.15 . 355 . 40 MET CA C 54.49 0.15 . 356 . 40 MET CB C 36.18 0.15 . 357 . 40 MET CE C 18.60 0.15 . 358 . 40 MET N N 121.02 0.1 . 359 . 41 GLU H H 8.67 0.02 . 360 . 41 GLU HA H 4.90 0.02 . 361 . 41 GLU HB2 H 1.93 0.02 . 362 . 41 GLU HB3 H 1.93 0.02 . 363 . 41 GLU HG2 H 2.23 0.02 . 364 . 41 GLU HG3 H 2.23 0.02 . 365 . 41 GLU C C 176.10 0.15 . 366 . 41 GLU CA C 55.71 0.15 . 367 . 41 GLU CB C 30.25 0.15 . 368 . 41 GLU N N 124.12 0.1 . 369 . 42 VAL H H 8.73 0.02 . 370 . 42 VAL HA H 4.12 0.02 . 371 . 42 VAL HB H 1.64 0.02 . 372 . 42 VAL HG1 H 0.93 0.02 . 373 . 42 VAL HG2 H 0.81 0.02 . 374 . 42 VAL C C 174.48 0.15 . 375 . 42 VAL CA C 61.38 0.15 . 376 . 42 VAL CB C 35.45 0.15 . 377 . 42 VAL CG1 C 22.20 0.15 . 378 . 42 VAL CG2 C 22.70 0.15 . 379 . 42 VAL N N 126.97 0.1 . 380 . 43 ALA H H 9.06 0.02 . 381 . 43 ALA HA H 4.34 0.02 . 382 . 43 ALA HB H 1.37 0.02 . 383 . 43 ALA C C 178.01 0.15 . 384 . 43 ALA CA C 52.16 0.15 . 385 . 43 ALA CB C 19.25 0.15 . 386 . 43 ALA N N 131.58 0.1 . 387 . 44 GLU H H 8.72 0.02 . 388 . 44 GLU HA H 4.04 0.02 . 389 . 44 GLU HB2 H 1.96 0.02 . 390 . 44 GLU HB3 H 1.96 0.02 . 391 . 44 GLU HG2 H 2.29 0.02 . 392 . 44 GLU HG3 H 2.29 0.02 . 393 . 44 GLU C C 178.43 0.15 . 394 . 44 GLU CA C 59.17 0.15 . 395 . 44 GLU CB C 29.10 0.15 . 396 . 44 GLU N N 119.53 0.1 . 397 . 45 GLY H H 8.88 0.02 . 398 . 45 GLY HA2 H 4.03 0.02 . 399 . 45 GLY HA3 H 3.65 0.02 . 400 . 45 GLY C C 172.91 0.15 . 401 . 45 GLY CA C 45.32 0.15 . 402 . 45 GLY N N 113.46 0.1 . 403 . 46 GLU H H 7.84 0.02 . 404 . 46 GLU HA H 4.13 0.02 . 405 . 46 GLU HB2 H 1.74 0.02 . 406 . 46 GLU HB3 H 2.27 0.02 . 407 . 46 GLU C C 175.19 0.15 . 408 . 46 GLU CA C 54.96 0.15 . 409 . 46 GLU CB C 31.44 0.15 . 410 . 46 GLU N N 123.32 0.1 . 411 . 47 TYR H H 8.45 0.02 . 412 . 47 TYR HA H 5.14 0.02 . 413 . 47 TYR HB2 H 2.76 0.02 . 414 . 47 TYR HB3 H 3.16 0.02 . 415 . 47 TYR HD1 H 6.91 0.02 . 416 . 47 TYR HD2 H 6.91 0.02 . 417 . 47 TYR HE1 H 6.84 0.02 . 418 . 47 TYR HE2 H 6.84 0.02 . 419 . 47 TYR C C 178.79 0.15 . 420 . 47 TYR CA C 55.36 0.15 . 421 . 47 TYR CB C 38.31 0.15 . 422 . 47 TYR N N 122.48 0.1 . 423 . 48 ILE H H 9.11 0.02 . 424 . 48 ILE HA H 3.52 0.02 . 425 . 48 ILE HB H 1.80 0.02 . 426 . 48 ILE HG12 H 1.08 0.02 . 427 . 48 ILE HG13 H 2.16 0.02 . 428 . 48 ILE HD1 H 0.88 0.02 . 429 . 48 ILE C C 176.66 0.15 . 430 . 48 ILE CA C 66.12 0.15 . 431 . 48 ILE CB C 38.62 0.15 . 432 . 48 ILE CD1 C 14.20 0.15 . 433 . 48 ILE N N 123.01 0.1 . 434 . 49 LEU H H 7.93 0.02 . 435 . 49 LEU HA H 3.94 0.02 . 436 . 49 LEU HB2 H 2.27 0.02 . 437 . 49 LEU HB3 H 2.27 0.02 . 438 . 49 LEU HG H 1.07 0.02 . 439 . 49 LEU C C 177.09 0.15 . 440 . 49 LEU CA C 58.52 0.15 . 441 . 49 LEU CB C 42.57 0.15 . 442 . 49 LEU N N 117.24 0.1 . 443 . 50 GLU H H 6.58 0.02 . 444 . 50 GLU HA H 4.13 0.02 . 445 . 50 GLU HB2 H 2.17 0.02 . 446 . 50 GLU HB3 H 2.17 0.02 . 447 . 50 GLU C C 179.36 0.15 . 448 . 50 GLU CA C 59.08 0.15 . 449 . 50 GLU CB C 29.04 0.15 . 450 . 50 GLU N N 115.11 0.1 . 451 . 51 ALA H H 7.84 0.02 . 452 . 51 ALA HA H 4.13 0.02 . 453 . 51 ALA HB H 1.45 0.02 . 454 . 51 ALA C C 179.75 0.15 . 455 . 51 ALA CA C 55.32 0.15 . 456 . 51 ALA CB C 19.31 0.15 . 457 . 51 ALA N N 124.91 0.1 . 458 . 52 ALA H H 7.72 0.02 . 459 . 52 ALA HA H 3.41 0.02 . 460 . 52 ALA C C 180.57 0.15 . 461 . 52 ALA CA C 55.21 0.15 . 462 . 52 ALA CB C 15.07 0.15 . 463 . 52 ALA N N 122.66 0.1 . 464 . 53 GLU H H 8.20 0.02 . 465 . 53 GLU HA H 4.11 0.02 . 466 . 53 GLU HB2 H 2.16 0.02 . 467 . 53 GLU HB3 H 2.16 0.02 . 468 . 53 GLU C C 181.64 0.15 . 469 . 53 GLU CA C 59.10 0.15 . 470 . 53 GLU CB C 28.99 0.15 . 471 . 53 GLU N N 118.94 0.1 . 472 . 54 ALA H H 8.14 0.02 . 473 . 54 ALA HA H 4.17 0.02 . 474 . 54 ALA HB H 1.53 0.02 . 475 . 54 ALA C C 179.55 0.15 . 476 . 54 ALA CA C 54.52 0.15 . 477 . 54 ALA CB C 17.83 0.15 . 478 . 54 ALA N N 124.63 0.1 . 479 . 55 GLN H H 7.18 0.02 . 480 . 55 GLN HA H 4.05 0.02 . 481 . 55 GLN HB2 H 1.26 0.02 . 482 . 55 GLN HB3 H 1.75 0.02 . 483 . 55 GLN HG2 H 2.42 0.02 . 484 . 55 GLN HG3 H 2.42 0.02 . 485 . 55 GLN C C 175.59 0.15 . 486 . 55 GLN CA C 54.81 0.15 . 487 . 55 GLN CB C 28.30 0.15 . 488 . 55 GLN N N 115.69 0.1 . 489 . 56 GLY H H 7.71 0.02 . 490 . 56 GLY HA2 H 4.07 0.02 . 491 . 56 GLY HA3 H 3.66 0.02 . 492 . 56 GLY C C 174.42 0.15 . 493 . 56 GLY CA C 44.85 0.15 . 494 . 56 GLY N N 106.34 0.1 . 495 . 57 TYR H H 7.40 0.02 . 496 . 57 TYR HA H 4.95 0.02 . 497 . 57 TYR HB2 H 2.15 0.02 . 498 . 57 TYR HB3 H 3.08 0.02 . 499 . 57 TYR HD1 H 6.61 0.02 . 500 . 57 TYR HD2 H 6.61 0.02 . 501 . 57 TYR HE1 H 6.72 0.02 . 502 . 57 TYR HE2 H 6.72 0.02 . 503 . 57 TYR C C 175.46 0.15 . 504 . 57 TYR CA C 54.77 0.15 . 505 . 57 TYR CB C 38.56 0.15 . 506 . 57 TYR N N 120.97 0.1 . 507 . 58 ASP H H 9.14 0.02 . 508 . 58 ASP HA H 5.26 0.02 . 509 . 58 ASP HB2 H 2.75 0.02 . 510 . 58 ASP HB3 H 2.92 0.02 . 511 . 58 ASP C C 175.26 0.15 . 512 . 58 ASP CA C 52.79 0.15 . 513 . 58 ASP CB C 41.01 0.15 . 514 . 58 ASP N N 123.82 0.1 . 515 . 59 TRP H H 7.96 0.02 . 516 . 59 TRP HA H 5.10 0.02 . 517 . 59 TRP HB2 H 2.79 0.02 . 518 . 59 TRP HB3 H 2.79 0.02 . 519 . 59 TRP HD1 H 6.78 0.02 . 520 . 59 TRP HE1 H 8.68 0.02 . 521 . 59 TRP HE3 H 7.24 0.02 . 522 . 59 TRP HZ2 H 5.35 0.02 . 523 . 59 TRP HZ3 H 6.48 0.02 . 524 . 59 TRP HH2 H 6.23 0.02 . 525 . 59 TRP CA C 55.50 0.15 . 526 . 59 TRP CB C 29.06 0.15 . 527 . 59 TRP N N 126.55 0.1 . 528 . 72 ALA HA H 5.27 0.02 . 529 . 72 ALA HB H 1.18 0.02 . 530 . 72 ALA C C 176.38 0.15 . 531 . 72 ALA CA C 54.09 0.15 . 532 . 72 ALA CB C 20.08 0.15 . 533 . 73 SER H H 9.01 0.02 . 534 . 73 SER HA H 5.27 0.02 . 535 . 73 SER HB2 H 3.78 0.02 . 536 . 73 SER HB3 H 3.78 0.02 . 537 . 73 SER C C 171.03 0.15 . 538 . 73 SER CA C 57.19 0.15 . 539 . 73 SER CB C 69.16 0.15 . 540 . 73 SER N N 118.00 0.1 . 541 . 74 ILE H H 9.16 0.02 . 542 . 74 ILE HA H 5.15 0.02 . 543 . 74 ILE HB H 2.06 0.02 . 544 . 74 ILE HG12 H 1.46 0.02 . 545 . 74 ILE HG13 H 1.46 0.02 . 546 . 74 ILE HG2 H 1.08 0.02 . 547 . 74 ILE HD1 H 0.88 0.02 . 548 . 74 ILE C C 177.13 0.15 . 549 . 74 ILE CA C 57.57 0.15 . 550 . 74 ILE CB C 39.64 0.15 . 551 . 74 ILE CG1 C 27.10 0.15 . 552 . 74 ILE CG2 C 17.60 0.15 . 553 . 74 ILE CD1 C 10.60 0.15 . 554 . 74 ILE N N 121.02 0.1 . 555 . 75 VAL H H 9.19 0.02 . 556 . 75 VAL HA H 4.75 0.02 . 557 . 75 VAL HB H 1.79 0.02 . 558 . 75 VAL HG1 H 0.87 0.02 . 559 . 75 VAL HG2 H 1.09 0.02 . 560 . 75 VAL C C 174.19 0.15 . 561 . 75 VAL CA C 60.83 0.15 . 562 . 75 VAL CB C 34.16 0.15 . 563 . 75 VAL N N 127.09 0.1 . 564 . 76 LYS H H 8.94 0.02 . 565 . 76 LYS HA H 4.58 0.02 . 566 . 76 LYS HB2 H 1.62 0.02 . 567 . 76 LYS HB3 H 2.18 0.02 . 568 . 76 LYS C C 176.42 0.15 . 569 . 76 LYS CA C 54.76 0.15 . 570 . 76 LYS CB C 33.64 0.15 . 571 . 76 LYS N N 127.64 0.1 . 572 . 77 GLU H H 7.77 0.02 . 573 . 77 GLU HA H 4.58 0.02 . 574 . 77 GLU HB2 H 1.68 0.02 . 575 . 77 GLU HB3 H 1.88 0.02 . 576 . 77 GLU HG2 H 2.30 0.02 . 577 . 77 GLU HG3 H 2.30 0.02 . 578 . 77 GLU C C 175.51 0.15 . 579 . 77 GLU CA C 56.65 0.15 . 580 . 77 GLU CB C 33.58 0.15 . 581 . 77 GLU N N 119.50 0.1 . 582 . 78 GLY H H 8.96 0.02 . 583 . 78 GLY HA2 H 4.49 0.02 . 584 . 78 GLY HA3 H 3.80 0.02 . 585 . 78 GLY C C 171.60 0.15 . 586 . 78 GLY CA C 44.91 0.15 . 587 . 78 GLY N N 112.64 0.1 . 588 . 79 GLU H H 6.34 0.02 . 589 . 79 GLU HA H 4.99 0.02 . 590 . 79 GLU HB2 H 1.90 0.02 . 591 . 79 GLU HB3 H 1.90 0.02 . 592 . 79 GLU HG2 H 1.76 0.02 . 593 . 79 GLU HG3 H 1.76 0.02 . 594 . 79 GLU C C 174.41 0.15 . 595 . 79 GLU CA C 54.14 0.15 . 596 . 79 GLU CB C 33.39 0.15 . 597 . 79 GLU N N 116.35 0.1 . 598 . 80 ILE H H 10.31 0.02 . 599 . 80 ILE HA H 4.55 0.02 . 600 . 80 ILE HB H 1.33 0.02 . 601 . 80 ILE HG12 H 0.88 0.02 . 602 . 80 ILE HG13 H 1.61 0.02 . 603 . 80 ILE HG2 H 0.77 0.02 . 604 . 80 ILE HD1 H 0.68 0.02 . 605 . 80 ILE C C 174.69 0.15 . 606 . 80 ILE CA C 60.39 0.15 . 607 . 80 ILE CB C 43.62 0.15 . 608 . 80 ILE CG2 C 16.86 0.15 . 609 . 80 ILE CD1 C 14.40 0.15 . 610 . 80 ILE N N 127.22 0.1 . 611 . 81 ASP H H 8.80 0.02 . 612 . 81 ASP HA H 4.95 0.02 . 613 . 81 ASP HB2 H 2.54 0.02 . 614 . 81 ASP HB3 H 2.77 0.02 . 615 . 81 ASP C C 175.83 0.15 . 616 . 81 ASP CA C 53.73 0.15 . 617 . 81 ASP CB C 42.28 0.15 . 618 . 81 ASP N N 128.92 0.1 . 619 . 82 MET H H 9.11 0.02 . 620 . 82 MET HA H 5.45 0.02 . 621 . 82 MET HB2 H 2.25 0.02 . 622 . 82 MET HB3 H 2.25 0.02 . 623 . 82 MET C C 176.34 0.15 . 624 . 82 MET CA C 54.85 0.15 . 625 . 82 MET CB C 36.91 0.15 . 626 . 82 MET N N 122.04 0.1 . 627 . 83 ASP H H 7.87 0.02 . 628 . 83 ASP HA H 4.73 0.02 . 629 . 83 ASP HB2 H 2.65 0.02 . 630 . 83 ASP HB3 H 2.99 0.02 . 631 . 83 ASP C C 174.45 0.15 . 632 . 83 ASP CA C 54.83 0.15 . 633 . 83 ASP CB C 41.17 0.15 . 634 . 83 ASP N N 122.20 0.1 . 635 . 84 MET H H 8.21 0.02 . 636 . 84 MET HA H 4.29 0.02 . 637 . 84 MET HB2 H 1.41 0.02 . 638 . 84 MET HB3 H 1.41 0.02 . 639 . 84 MET C C 175.35 0.15 . 640 . 84 MET CA C 57.24 0.15 . 641 . 84 MET CB C 31.76 0.15 . 642 . 84 MET N N 117.98 0.1 . 643 . 85 GLN H H 8.36 0.02 . 644 . 85 GLN HA H 4.68 0.02 . 645 . 85 GLN HB2 H 2.08 0.02 . 646 . 85 GLN HB3 H 2.08 0.02 . 647 . 85 GLN C C 175.35 0.15 . 648 . 85 GLN CA C 54.95 0.15 . 649 . 85 GLN CB C 29.13 0.15 . 650 . 85 GLN N N 120.30 0.1 . 651 . 86 GLN H H 8.82 0.02 . 652 . 86 GLN CA C 54.85 0.15 . 653 . 86 GLN CB C 30.74 0.15 . 654 . 86 GLN N N 119.29 0.1 . 655 . 87 ILE HA H 4.76 0.02 . 656 . 87 ILE C C 174.94 0.15 . 657 . 87 ILE CA C 59.06 0.15 . 658 . 88 LEU H H 9.58 0.02 . 659 . 88 LEU HA H 4.74 0.02 . 660 . 88 LEU C C 178.09 0.15 . 661 . 88 LEU CA C 53.49 0.15 . 662 . 88 LEU CB C 43.40 0.15 . 663 . 88 LEU N N 126.54 0.1 . 664 . 89 SER H H 9.39 0.02 . 665 . 89 SER HA H 4.54 0.02 . 666 . 89 SER HB2 H 4.04 0.02 . 667 . 89 SER HB3 H 4.04 0.02 . 668 . 89 SER C C 174.71 0.15 . 669 . 89 SER CA C 57.05 0.15 . 670 . 89 SER CB C 65.66 0.15 . 671 . 89 SER N N 122.06 0.1 . 672 . 90 ASP H H 9.01 0.02 . 673 . 90 ASP HA H 4.45 0.02 . 674 . 90 ASP HB2 H 2.66 0.02 . 675 . 90 ASP HB3 H 2.76 0.02 . 676 . 90 ASP C C 178.20 0.15 . 677 . 90 ASP CA C 57.65 0.15 . 678 . 90 ASP CB C 39.63 0.15 . 679 . 90 ASP N N 122.03 0.1 . 680 . 91 GLU H H 8.59 0.02 . 681 . 91 GLU HA H 4.10 0.02 . 682 . 91 GLU HB2 H 1.93 0.02 . 683 . 91 GLU HB3 H 1.93 0.02 . 684 . 91 GLU HG2 H 2.11 0.02 . 685 . 91 GLU HG3 H 2.11 0.02 . 686 . 91 GLU C C 179.82 0.15 . 687 . 91 GLU CA C 59.81 0.15 . 688 . 91 GLU CB C 29.65 0.15 . 689 . 91 GLU N N 119.86 0.1 . 690 . 92 GLU H H 8.08 0.02 . 691 . 92 GLU HA H 3.70 0.02 . 692 . 92 GLU HB2 H 1.72 0.02 . 693 . 92 GLU HB3 H 1.72 0.02 . 694 . 92 GLU C C 177.68 0.15 . 695 . 92 GLU CA C 59.63 0.15 . 696 . 92 GLU CB C 28.88 0.15 . 697 . 92 GLU N N 121.74 0.1 . 698 . 93 VAL H H 8.01 0.02 . 699 . 93 VAL HA H 3.96 0.02 . 700 . 93 VAL HB H 2.25 0.02 . 701 . 93 VAL HG1 H 0.99 0.02 . 702 . 93 VAL HG2 H 1.08 0.02 . 703 . 93 VAL C C 179.68 0.15 . 704 . 93 VAL CA C 66.29 0.15 . 705 . 93 VAL CB C 33.35 0.15 . 706 . 93 VAL N N 117.64 0.1 . 707 . 94 GLU H H 9.21 0.02 . 708 . 94 GLU HA H 4.28 0.02 . 709 . 94 GLU HB2 H 2.19 0.02 . 710 . 94 GLU HB3 H 2.19 0.02 . 711 . 94 GLU C C 177.74 0.15 . 712 . 94 GLU CA C 59.35 0.15 . 713 . 94 GLU CB C 30.94 0.15 . 714 . 94 GLU N N 117.75 0.1 . 715 . 95 GLU H H 8.48 0.02 . 716 . 95 GLU HA H 4.68 0.02 . 717 . 95 GLU C C 178.14 0.15 . 718 . 95 GLU CA C 57.19 0.15 . 719 . 95 GLU CB C 30.81 0.15 . 720 . 95 GLU N N 115.57 0.1 . 721 . 96 LYS H H 7.38 0.02 . 722 . 96 LYS HA H 4.53 0.02 . 723 . 96 LYS HB2 H 2.28 0.02 . 724 . 96 LYS HB3 H 2.28 0.02 . 725 . 96 LYS C C 175.12 0.15 . 726 . 96 LYS CA C 56.24 0.15 . 727 . 96 LYS CB C 32.65 0.15 . 728 . 96 LYS N N 115.68 0.1 . 729 . 97 ASP H H 6.90 0.02 . 730 . 97 ASP HA H 4.40 0.02 . 731 . 97 ASP HB2 H 3.19 0.02 . 732 . 97 ASP HB3 H 3.46 0.02 . 733 . 97 ASP C C 174.70 0.15 . 734 . 97 ASP CA C 56.27 0.15 . 735 . 97 ASP CB C 39.16 0.15 . 736 . 97 ASP N N 111.47 0.1 . 737 . 98 VAL H H 8.31 0.02 . 738 . 98 VAL HA H 4.62 0.02 . 739 . 98 VAL HB H 1.76 0.02 . 740 . 98 VAL HG1 H 0.98 0.02 . 741 . 98 VAL HG2 H 1.13 0.02 . 742 . 98 VAL C C 177.87 0.15 . 743 . 98 VAL CA C 63.09 0.15 . 744 . 98 VAL CB C 31.68 0.15 . 745 . 98 VAL N N 118.00 0.1 . 746 . 99 ARG H H 9.32 0.02 . 747 . 99 ARG HA H 4.91 0.02 . 748 . 99 ARG CA C 52.30 0.15 . 749 . 99 ARG CB C 33.48 0.15 . 750 . 99 ARG N N 124.29 0.1 . 751 . 104 GLY HA2 H 5.50 0.02 . 752 . 104 GLY HA3 H 3.47 0.02 . 753 . 104 GLY C C 171.56 0.15 . 754 . 104 GLY CA C 44.85 0.15 . 755 . 105 SER H H 9.24 0.02 . 756 . 105 SER HA H 5.64 0.02 . 757 . 105 SER HB2 H 3.61 0.02 . 758 . 105 SER HB3 H 3.73 0.02 . 759 . 105 SER CA C 54.69 0.15 . 760 . 105 SER CB C 66.04 0.15 . 761 . 105 SER N N 121.89 0.1 . 762 . 106 PRO HA H 4.44 0.02 . 763 . 106 PRO HB2 H 2.04 0.02 . 764 . 106 PRO HB3 H 2.04 0.02 . 765 . 106 PRO C C 176.14 0.15 . 766 . 106 PRO CA C 64.19 0.15 . 767 . 106 PRO CB C 32.62 0.15 . 768 . 107 ALA H H 8.75 0.02 . 769 . 107 ALA HA H 4.77 0.02 . 770 . 107 ALA HB H 1.18 0.02 . 771 . 107 ALA C C 175.10 0.15 . 772 . 107 ALA CA C 50.64 0.15 . 773 . 107 ALA CB C 20.09 0.15 . 774 . 107 ALA N N 127.87 0.1 . 775 . 108 ALA H H 7.54 0.02 . 776 . 108 ALA HA H 4.57 0.02 . 777 . 108 ALA HB H 1.54 0.02 . 778 . 108 ALA C C 175.40 0.15 . 779 . 108 ALA CA C 50.56 0.15 . 780 . 108 ALA CB C 23.30 0.15 . 781 . 108 ALA N N 120.17 0.1 . 782 . 109 ASP H H 8.50 0.02 . 783 . 109 ASP HA H 4.38 0.02 . 784 . 109 ASP HB2 H 2.72 0.02 . 785 . 109 ASP HB3 H 2.72 0.02 . 786 . 109 ASP C C 176.37 0.15 . 787 . 109 ASP CA C 57.72 0.15 . 788 . 109 ASP CB C 41.29 0.15 . 789 . 109 ASP N N 117.22 0.1 . 790 . 110 GLU H H 7.56 0.02 . 791 . 110 GLU HA H 5.04 0.02 . 792 . 110 GLU HB2 H 1.91 0.02 . 793 . 110 GLU HB3 H 1.91 0.02 . 794 . 110 GLU HG2 H 2.11 0.02 . 795 . 110 GLU HG3 H 2.19 0.02 . 796 . 110 GLU C C 174.69 0.15 . 797 . 110 GLU CA C 55.56 0.15 . 798 . 110 GLU CB C 32.14 0.15 . 799 . 110 GLU N N 117.21 0.1 . 800 . 111 VAL H H 8.70 0.02 . 801 . 111 VAL HA H 4.71 0.02 . 802 . 111 VAL HB H 2.05 0.02 . 803 . 111 VAL HG1 H 1.09 0.02 . 804 . 111 VAL HG2 H 1.02 0.02 . 805 . 111 VAL C C 175.04 0.15 . 806 . 111 VAL CA C 59.81 0.15 . 807 . 111 VAL CB C 36.12 0.15 . 808 . 111 VAL CG1 C 23.00 0.15 . 809 . 111 VAL CG2 C 22.40 0.15 . 810 . 111 VAL N N 124.49 0.1 . 811 . 112 LYS H H 8.52 0.02 . 812 . 112 LYS HA H 5.67 0.02 . 813 . 112 LYS HB2 H 1.11 0.02 . 814 . 112 LYS HB3 H 1.11 0.02 . 815 . 112 LYS C C 176.65 0.15 . 816 . 112 LYS CA C 55.04 0.15 . 817 . 112 LYS CB C 34.63 0.15 . 818 . 112 LYS N N 126.40 0.1 . 819 . 113 ILE H H 9.53 0.02 . 820 . 113 ILE HA H 5.78 0.02 . 821 . 113 ILE HB H 1.78 0.02 . 822 . 113 ILE HG12 H 1.22 0.02 . 823 . 113 ILE HG13 H 1.84 0.02 . 824 . 113 ILE HG2 H 0.95 0.02 . 825 . 113 ILE HD1 H 1.03 0.02 . 826 . 113 ILE C C 174.47 0.15 . 827 . 113 ILE CA C 58.64 0.15 . 828 . 113 ILE CB C 43.16 0.15 . 829 . 113 ILE CG2 C 19.04 0.15 . 830 . 113 ILE CD1 C 14.11 0.15 . 831 . 113 ILE N N 116.24 0.1 . 832 . 114 VAL H H 9.29 0.02 . 833 . 114 VAL HA H 5.55 0.02 . 834 . 114 VAL HB H 2.20 0.02 . 835 . 114 VAL HG1 H 1.11 0.02 . 836 . 114 VAL HG2 H 1.22 0.02 . 837 . 114 VAL C C 177.50 0.15 . 838 . 114 VAL CA C 61.10 0.15 . 839 . 114 VAL CB C 32.92 0.15 . 840 . 114 VAL CG1 C 21.30 0.15 . 841 . 114 VAL CG2 C 22.00 0.15 . 842 . 114 VAL N N 124.33 0.1 . 843 . 115 TYR H H 8.92 0.02 . 844 . 115 TYR HA H 4.82 0.02 . 845 . 115 TYR HB2 H 3.24 0.02 . 846 . 115 TYR HB3 H 3.24 0.02 . 847 . 115 TYR HD1 H 6.29 0.02 . 848 . 115 TYR HD2 H 6.29 0.02 . 849 . 115 TYR HE1 H 6.39 0.02 . 850 . 115 TYR HE2 H 6.39 0.02 . 851 . 115 TYR C C 173.17 0.15 . 852 . 115 TYR CA C 55.28 0.15 . 853 . 115 TYR CB C 38.13 0.15 . 854 . 115 TYR N N 128.93 0.1 . 855 . 116 ASN H H 9.74 0.02 . 856 . 116 ASN HA H 5.22 0.02 . 857 . 116 ASN HB2 H 1.89 0.02 . 858 . 116 ASN HB3 H 3.38 0.02 . 859 . 116 ASN HD21 H 6.63 0.02 . 860 . 116 ASN HD22 H 7.69 0.02 . 861 . 116 ASN C C 175.43 0.15 . 862 . 116 ASN CA C 53.31 0.15 . 863 . 116 ASN CB C 37.70 0.15 . 864 . 116 ASN N N 120.72 0.1 . 865 . 116 ASN ND2 N 107.29 0.1 . 866 . 117 ALA H H 7.02 0.02 . 867 . 117 ALA HA H 3.55 0.02 . 868 . 117 ALA HB H 1.00 0.02 . 869 . 117 ALA C C 175.74 0.15 . 870 . 117 ALA CA C 52.32 0.15 . 871 . 117 ALA CB C 17.45 0.15 . 872 . 117 ALA N N 115.11 0.1 . 873 . 118 ALY H H 8.82 0.02 . 874 . 118 ALY HCA H 3.57 0.02 . 875 . 118 ALY HB2 H 2.05 0.02 . 876 . 118 ALY HB3 H 2.05 0.02 . 877 . 118 ALY HG2 H 0.12 0.02 . 878 . 118 ALY HG3 H 0.12 0.02 . 879 . 118 ALY HD2 H 1.22 0.02 . 880 . 118 ALY HD3 H 1.66 0.02 . 881 . 118 ALY HE2 H 2.78 0.02 . 882 . 118 ALY HE3 H 2.96 0.02 . 883 . 118 ALY HZ H 7.79 0.02 . 884 . 118 ALY C C 173.85 0.15 . 885 . 118 ALY CA C 57.97 0.15 . 886 . 118 ALY CB C 30.43 0.15 . 887 . 118 ALY CG C 22.13 0.15 . 888 . 118 ALY CD C 31.27 0.15 . 889 . 118 ALY CE C 41.75 0.15 . 890 . 118 ALY N N 118.38 0.1 . 891 . 118 ALY NZ N 126.40 0.1 . 892 . 118 ALY HH31 H 1.91 0.1 . 893 . 118 ALY HH32 H 1.91 0.1 . 894 . 118 ALY HH33 H 1.91 0.1 . 895 . 118 ALY CH3 C 24.70 0.15 . 896 . 118 ALY CH C 176.40 0.15 . 897 . 119 HIS H H 5.93 0.02 . 898 . 119 HIS HA H 4.02 0.02 . 899 . 119 HIS HB2 H 2.41 0.02 . 900 . 119 HIS HB3 H 3.32 0.02 . 901 . 119 HIS HD2 H 7.53 0.02 . 902 . 119 HIS HE1 H 8.16 0.02 . 903 . 119 HIS C C 175.75 0.15 . 904 . 119 HIS CA C 57.14 0.15 . 905 . 119 HIS CB C 31.15 0.15 . 906 . 119 HIS N N 114.22 0.1 . 907 . 120 LEU H H 7.72 0.02 . 908 . 120 LEU HA H 3.91 0.02 . 909 . 120 LEU HB2 H 0.62 0.02 . 910 . 120 LEU HB3 H 0.62 0.02 . 911 . 120 LEU C C 178.99 0.15 . 912 . 120 LEU CA C 55.88 0.15 . 913 . 120 LEU CB C 41.74 0.15 . 914 . 120 LEU N N 123.76 0.1 . 915 . 121 ASP H H 8.79 0.02 . 916 . 121 ASP HA H 4.06 0.02 . 917 . 121 ASP HB2 H 2.82 0.02 . 918 . 121 ASP HB3 H 2.82 0.02 . 919 . 121 ASP C C 179.29 0.15 . 920 . 121 ASP CA C 57.65 0.15 . 921 . 121 ASP CB C 39.74 0.15 . 922 . 121 ASP N N 123.48 0.1 . 923 . 122 TYR H H 7.83 0.02 . 924 . 122 TYR HA H 4.47 0.02 . 925 . 122 TYR HB2 H 2.93 0.02 . 926 . 122 TYR HB3 H 3.31 0.02 . 927 . 122 TYR HD1 H 7.13 0.02 . 928 . 122 TYR HD2 H 7.13 0.02 . 929 . 122 TYR HE1 H 6.69 0.02 . 930 . 122 TYR HE2 H 6.69 0.02 . 931 . 122 TYR C C 175.84 0.15 . 932 . 122 TYR CA C 58.10 0.15 . 933 . 122 TYR CB C 36.79 0.15 . 934 . 122 TYR N N 114.68 0.1 . 935 . 123 LEU H H 6.97 0.02 . 936 . 123 LEU HA H 4.35 0.02 . 937 . 123 LEU HB2 H 1.11 0.02 . 938 . 123 LEU HB3 H 1.47 0.02 . 939 . 123 LEU HG H 0.87 0.02 . 940 . 123 LEU HD1 H 0.49 0.02 . 941 . 123 LEU HD2 H 0.67 0.02 . 942 . 123 LEU C C 177.89 0.15 . 943 . 123 LEU CA C 55.35 0.15 . 944 . 123 LEU CB C 42.23 0.15 . 945 . 123 LEU CD1 C 22.05 0.15 . 946 . 123 LEU CD2 C 26.00 0.15 . 947 . 123 LEU N N 120.28 0.1 . 948 . 124 GLN H H 7.12 0.02 . 949 . 124 GLN HA H 3.74 0.02 . 950 . 124 GLN HB2 H 2.10 0.02 . 951 . 124 GLN HB3 H 2.10 0.02 . 952 . 124 GLN HG2 H 2.46 0.02 . 953 . 124 GLN HG3 H 2.46 0.02 . 954 . 124 GLN C C 177.10 0.15 . 955 . 124 GLN CA C 59.38 0.15 . 956 . 124 GLN CB C 29.26 0.15 . 957 . 124 GLN N N 117.08 0.1 . 958 . 125 ASN H H 8.39 0.02 . 959 . 125 ASN HA H 4.48 0.02 . 960 . 125 ASN HB2 H 2.95 0.02 . 961 . 125 ASN HB3 H 3.11 0.02 . 962 . 125 ASN HD21 H 7.05 0.02 . 963 . 125 ASN HD22 H 7.65 0.02 . 964 . 125 ASN C C 176.45 0.15 . 965 . 125 ASN CA C 54.86 0.15 . 966 . 125 ASN CB C 36.35 0.15 . 967 . 125 ASN N N 116.94 0.1 . 968 . 125 ASN ND2 N 112.31 0.1 . 969 . 126 ARG H H 7.94 0.02 . 970 . 126 ARG HA H 4.51 0.02 . 971 . 126 ARG C C 175.33 0.15 . 972 . 126 ARG CA C 55.45 0.15 . 973 . 126 ARG CB C 31.90 0.15 . 974 . 126 ARG N N 121.58 0.1 . 975 . 127 VAL H H 7.27 0.02 . 976 . 127 VAL HA H 4.17 0.02 . 977 . 127 VAL CA C 62.65 0.15 . 978 . 127 VAL CB C 32.29 0.15 . 979 . 127 VAL N N 125.84 0.1 . stop_ save_